FLEQ_PSEAE
ID FLEQ_PSEAE Reviewed; 490 AA.
AC G3XCV0;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Transcriptional regulator FleQ {ECO:0000303|PubMed:9287015};
GN Name=fleQ {ECO:0000303|PubMed:9287015}; OrderedLocusNames=PA1097;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9287015; DOI=10.1128/jb.179.17.5574-5581.1997;
RA Arora S.K., Ritchings B.W., Almira E.C., Lory S., Ramphal R.;
RT "A transcriptional activator, FleQ, regulates mucin adhesion and flagellar
RT gene expression in Pseudomonas aeruginosa in a cascade manner.";
RL J. Bacteriol. 179:5574-5581(1997).
RN [3]
RP FUNCTION.
RC STRAIN=PAK;
RX PubMed=11673434; DOI=10.1128/jb.183.22.6636-6644.2001;
RA Dasgupta N., Ramphal R.;
RT "Interaction of the antiactivator FleN with the transcriptional activator
RT FleQ regulates flagellar number in Pseudomonas aeruginosa.";
RL J. Bacteriol. 183:6636-6644(2001).
RN [4]
RP FUNCTION, AND INTERACTION WITH FLEN.
RX PubMed=22581773; DOI=10.1093/nar/gks384;
RA Baraquet C., Murakami K., Parsek M.R., Harwood C.S.;
RT "The FleQ protein from Pseudomonas aeruginosa functions as both a repressor
RT and an activator to control gene expression from the pel operon promoter in
RT response to c-di-GMP.";
RL Nucleic Acids Res. 40:7207-7218(2012).
RN [5] {ECO:0007744|PDB:4WXM}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-139, FUNCTION, DOMAIN,
RP DISRUPTION PHENOTYPE, SUBUNIT, AND MUTAGENESIS OF PHE-26; HIS-119; ARG-144
RP AND ARG-185.
RX PubMed=26362077; DOI=10.1016/j.jsb.2015.09.002;
RA Su T., Liu S., Wang K., Chi K., Zhu D., Wei T., Huang Y., Guo L., Hu W.,
RA Xu S., Lin Z., Gu L.;
RT "The REC domain mediated dimerization is critical for FleQ from Pseudomonas
RT aeruginosa to function as a c-di-GMP receptor and flagella gene
RT regulator.";
RL J. Struct. Biol. 192:1-13(2015).
RN [6] {ECO:0007744|PDB:5EXP, ECO:0007744|PDB:5EXS, ECO:0007744|PDB:5EXT}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 137-394 IN COMPLEX WITH ADP AND
RP CYCLIC DIGUANOSINE MONOPHOSPHATE, SUBUNIT, ACTIVITY REGULATION, AND
RP MUTAGENESIS OF ARG-185; ASN-186; GLU-330 AND ARG-334.
RX PubMed=26712005; DOI=10.1073/pnas.1523148113;
RA Matsuyama B.Y., Krasteva P.V., Baraquet C., Harwood C.S., Sondermann H.,
RA Navarro M.V.;
RT "Mechanistic insights into c-di-GMP-dependent control of the biofilm
RT regulator FleQ from Pseudomonas aeruginosa.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E209-E218(2016).
CC -!- FUNCTION: AAA+ ATPase enhancer-binding protein that acts as a
CC transcription regulator and plays a role in the modulation of mucin
CC adhesion and flagellar gene expression (PubMed:9287015,
CC PubMed:11673434, PubMed:26362077). In addition to flagella genes,
CC regulates also expression of biofilm-related genes (PubMed:22581773).
CC Functions as a transcriptional repressor in the absence of c-di-GMP and
CC as an activator when c-di-GMP is present (PubMed:22581773).
CC {ECO:0000269|PubMed:11673434, ECO:0000269|PubMed:22581773,
CC ECO:0000269|PubMed:26362077, ECO:0000269|PubMed:9287015}.
CC -!- ACTIVITY REGULATION: C-di-GMP interaction leads to active site
CC obstruction, hexameric ring destabilization thus relieving DNA bending
CC and activating gene transcription. {ECO:0000269|PubMed:26712005}.
CC -!- SUBUNIT: Forms homodimers (PubMed:26362077). Forms homohexamers that
CC inhibit transcription initiation (PubMed:26712005). Interacts with
CC FleN; this complex is formed in the presence as well as in the absence
CC of c-di-GMP or ATP (PubMed:22581773). {ECO:0000269|PubMed:22581773,
CC ECO:0000269|PubMed:26362077, ECO:0000269|PubMed:26712005}.
CC -!- DOMAIN: The N-terminal FleQ domain mediates dimerization and is
CC essential for function. {ECO:0000269|PubMed:26362077}.
CC -!- DISRUPTION PHENOTYPE: Deletion results in the concomitant loss of
CC motility, mucin adhesion, and the ability to synthesize flagellin.
CC {ECO:0000269|PubMed:26362077, ECO:0000269|PubMed:9287015}.
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DR EMBL; AE004091; AAG04486.1; -; Genomic_DNA.
DR PIR; B83508; B83508.
DR RefSeq; NP_249788.1; NC_002516.2.
DR RefSeq; WP_003086448.1; NZ_QZGE01000006.1.
DR PDB; 4WXM; X-ray; 2.30 A; A/B/C/D/E=1-139.
DR PDB; 5EXP; X-ray; 1.80 A; A=137-394.
DR PDB; 5EXS; X-ray; 2.50 A; A=137-394.
DR PDB; 5EXT; X-ray; 2.40 A; A=137-394.
DR PDB; 5EXX; X-ray; 3.31 A; A=137-477.
DR PDB; 6J7E; X-ray; 2.40 A; A=142-399.
DR PDB; 6JDI; X-ray; 1.95 A; A=142-399.
DR PDB; 6JDL; X-ray; 2.25 A; A=142-399.
DR PDB; 7EJW; X-ray; 1.98 A; C/D=142-395.
DR PDBsum; 4WXM; -.
DR PDBsum; 5EXP; -.
DR PDBsum; 5EXS; -.
DR PDBsum; 5EXT; -.
DR PDBsum; 5EXX; -.
DR PDBsum; 6J7E; -.
DR PDBsum; 6JDI; -.
DR PDBsum; 6JDL; -.
DR PDBsum; 7EJW; -.
DR AlphaFoldDB; G3XCV0; -.
DR SMR; G3XCV0; -.
DR STRING; 287.DR97_840; -.
DR PaxDb; G3XCV0; -.
DR PRIDE; G3XCV0; -.
DR EnsemblBacteria; AAG04486; AAG04486; PA1097.
DR GeneID; 881960; -.
DR KEGG; pae:PA1097; -.
DR PATRIC; fig|208964.12.peg.1136; -.
DR PseudoCAP; PA1097; -.
DR HOGENOM; CLU_000445_0_7_6; -.
DR InParanoid; G3XCV0; -.
DR OMA; LNYPQLT; -.
DR PhylomeDB; G3XCV0; -.
DR BioCyc; PAER208964:G1FZ6-1120-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR CollecTF; EXPREG_000004a0; -.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:PseudoCAP.
DR GO; GO:0035438; F:cyclic-di-GMP binding; IDA:PseudoCAP.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IMP:PseudoCAP.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IMP:PseudoCAP.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
DR GO; GO:1901202; P:negative regulation of extracellular matrix assembly; IMP:PseudoCAP.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IMP:PseudoCAP.
DR GO; GO:2000155; P:positive regulation of cilium-dependent cell motility; IMP:PseudoCAP.
DR GO; GO:1902021; P:regulation of bacterial-type flagellum-dependent cell motility; IMP:PseudoCAP.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:PseudoCAP.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:PseudoCAP.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR010518; FleQ.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR002197; HTH_Fis.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR InterPro; IPR025944; Sigma_54_int_dom_CS.
DR Pfam; PF06490; FleQ; 1.
DR Pfam; PF02954; HTH_8; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR PRINTS; PR01590; HTHFIS.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA-binding; Nucleotide-binding;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..490
FT /note="Transcriptional regulator FleQ"
FT /id="PRO_0000448537"
FT BINDING 142
FT /ligand="cyclic di-3',5'-guanylate"
FT /ligand_id="ChEBI:CHEBI:58805"
FT /evidence="ECO:0000269|PubMed:26712005,
FT ECO:0007744|PDB:5EXX"
FT BINDING 147
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:26712005,
FT ECO:0007744|PDB:5EXT"
FT BINDING 177..182
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:26712005,
FT ECO:0007744|PDB:5EXT"
FT BINDING 186..189
FT /ligand="cyclic di-3',5'-guanylate"
FT /ligand_id="ChEBI:CHEBI:58805"
FT /evidence="ECO:0000269|PubMed:26712005,
FT ECO:0007744|PDB:5EXX"
FT BINDING 330..341
FT /ligand="cyclic di-3',5'-guanylate"
FT /ligand_id="ChEBI:CHEBI:58805"
FT /evidence="ECO:0000269|PubMed:26712005,
FT ECO:0007744|PDB:5EXX"
FT BINDING 334
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:26712005,
FT ECO:0007744|PDB:5EXT"
FT BINDING 363
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:26712005,
FT ECO:0007744|PDB:5EXT"
FT MUTAGEN 26
FT /note="F->N: Almost complete loss of biofilm formation."
FT /evidence="ECO:0000269|PubMed:26362077"
FT MUTAGEN 119
FT /note="H->N: About 50% loss of biofilm formation."
FT /evidence="ECO:0000269|PubMed:26362077"
FT MUTAGEN 144
FT /note="R->A: Almost complete loss of biofilm formation."
FT /evidence="ECO:0000269|PubMed:26362077"
FT MUTAGEN 185
FT /note="R->A: Almost complete loss of biofilm formation."
FT /evidence="ECO:0000269|PubMed:26362077"
FT MUTAGEN 185
FT /note="R->E: More than 75% repressed pel transcription."
FT /evidence="ECO:0000269|PubMed:26712005"
FT MUTAGEN 186
FT /note="N->A: More than 75% repressed pel transcription."
FT /evidence="ECO:0000269|PubMed:26712005"
FT MUTAGEN 330
FT /note="E->A: More than 75% repressed pel transcription."
FT /evidence="ECO:0000269|PubMed:26712005"
FT MUTAGEN 334
FT /note="R->E: More than 75% repressed pel transcription."
FT /evidence="ECO:0000269|PubMed:26712005"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:4WXM"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:4WXM"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:4WXM"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:4WXM"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:4WXM"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:4WXM"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:4WXM"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:4WXM"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:4WXM"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:4WXM"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:4WXM"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:4WXM"
FT HELIX 111..128
FT /evidence="ECO:0007829|PDB:4WXM"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:5EXP"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:5EXP"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:5EXP"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:5EXP"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:5EXP"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:5EXP"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:5EXP"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:5EXT"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:5EXP"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:5EXP"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:5EXP"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:5EXP"
FT HELIX 252..264
FT /evidence="ECO:0007829|PDB:5EXP"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:5EXP"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:5EXT"
FT STRAND 281..288
FT /evidence="ECO:0007829|PDB:5EXP"
FT HELIX 290..295
FT /evidence="ECO:0007829|PDB:5EXP"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:5EXX"
FT HELIX 301..307
FT /evidence="ECO:0007829|PDB:5EXP"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:5EXP"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:5EXP"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:5EXP"
FT HELIX 324..337
FT /evidence="ECO:0007829|PDB:5EXP"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:5EXP"
FT HELIX 347..353
FT /evidence="ECO:0007829|PDB:5EXP"
FT HELIX 361..375
FT /evidence="ECO:0007829|PDB:5EXP"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:5EXP"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:5EXP"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:5EXP"
SQ SEQUENCE 490 AA; 55277 MW; 214CD52BC8F9C0AA CRC64;
MWRETKLLLI DDNLDRSRDL AVILNFLGED QLTCNSEDWR EVAAGLSNSR EALCVLLGSV
ESKGGAVELL KQLASWDEYL PILLIGEPAP ADWPEELRRR VLASLEMPPS YNKLLDSLHR
AQVYREMYDQ ARERGRSREP NLFRSLVGTS RAIQQVRQMM QQVADTDASV LILGESGTGK
EVVARNLHYH SKRREGPFVP VNCGAIPAEL LESELFGHEK GAFTGAITSR AGRFELANGG
TLFLDEIGDM PLPMQVKLLR VLQERTFERV GSNKTQNVDV RIIAATHKNL EKMIEDGTFR
EDLYYRLNVF PIEMAPLRER VEDIALLLNE LISRMEHEKR GSIRFNSAAI MSLCRHDWPG
NVRELANLVE RLAIMHPYGV IGVGELPKKF RHVDDEDEQL ASSLREELEE RAAINAGLPG
MDAPAMLPAE GLDLKDYLAN LEQGLIQQAL DDAGGVVARA AERLRIRRTT LVEKMRKYGM
SRRDDDLSDD
